Evidence map›Paper›PMID 26496431›Full record

ArticlePLoS genetics2015

A Role for the Chaperone Complex BAG3-HSPB8 in Actin Dynamics, Spindle Orientation and Proper Chromosome Segregation during Mitosis.

Margit Fuchs, Carole Luthold, Solenn M Guilbert, Alice Anaïs Varlet, Herman Lambert, Alexandra Jetté, Sabine Elowe, Jacques Landry, Josée N Lavoie

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.9field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed, 56 citations in OpenAlex.

  1. Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Margit FuchsCentre de Recherche sur le Cancer de l'Université Laval and Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval, Quebec, Canada; Oncology, Centre de Recherche du CHU de Québec-Université Laval, Quebec, Canada.
Carole LutholdCentre de Recherche sur le Cancer de l'Université Laval and Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval, Quebec, Canada; Oncology, Centre de Recherche du CHU de Québec-Université Laval, Quebec, Canada.
Solenn M GuilbertCentre de Recherche sur le Cancer de l'Université Laval and Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval, Quebec, Canada; Oncology, Centre de Recherche du CHU de Québec-Université Laval, Quebec, Canada.
Alice Anaïs VarletCentre de Recherche sur le Cancer de l'Université Laval and Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval, Quebec, Canada; Oncology, Centre de Recherche du CHU de Québec-Université Laval, Quebec, Canada.
Herman LambertCentre de Recherche sur le Cancer de l'Université Laval and Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval, Quebec, Canada; Oncology, Centre de Recherche du CHU de Québec-Université Laval, Quebec, Canada.
Alexandra JettéCentre de Recherche sur le Cancer de l'Université Laval and Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval, Quebec, Canada; Oncology, Centre de Recherche du CHU de Québec-Université Laval, Quebec, Canada.
Sabine EloweReproduction, Perinatal Health and Child Health, Centre de Recherche du CHU de Québec-Université Laval, Quebec, Canada; Centre de Recherche sur le Cancer de l'Université Laval and Département de Pédiatrie, Université Laval, Quebec, Canada.
Jacques LandryCentre de Recherche sur le Cancer de l'Université Laval and Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval, Quebec, Canada; Oncology, Centre de Recherche du CHU de Québec-Université Laval, Quebec, Canada.
Josée N LavoieCentre de Recherche sur le Cancer de l'Université Laval and Département de Biologie Moléculaire, Biochimie Médicale et Pathologie, Université Laval, Quebec, Canada; Oncology, Centre de Recherche du CHU de Québec-Université Laval, Quebec, Canada.
Université Laval · CACentre hospitalier de l'Université Laval · CA

Funding

Canadian Institutes of Health Research 7088
6 · The paper itself

Abstract

The co-chaperone BAG3, in complex with the heat shock protein HSPB8, plays a role in protein quality control during mechanical strain. It is part of a multichaperone complex that senses damaged cytoskeletal proteins and orchestrates their seclusion and/or degradation by selective autophagy. Here we describe a novel role for the BAG3-HSPB8 complex in mitosis, a process involving profound changes in cell tension homeostasis. BAG3 is hyperphosphorylated at mitotic entry and localizes to centrosomal regions. BAG3 regulates, in an HSPB8-dependent manner, the timely congression of chromosomes to the metaphase plate by influencing the three-dimensional positioning of the mitotic spindle. Depletion of BAG3 caused defects in cell rounding at metaphase and dramatic blebbing of the cortex associated with abnormal spindle rotations. Similar defects were observed upon silencing of the autophagic receptor p62/SQSTM1 that contributes to BAG3-mediated selective autophagy pathway. Mitotic cells depleted of BAG3, HSPB8 or p62/SQSTM1 exhibited disorganized actin-rich retraction fibres, which are proposed to guide spindle orientation. Proper spindle positioning was rescued in BAG3-depleted cells upon addition of the lectin concanavalin A, which restores cortex rigidity. Together, our findings suggest the existence of a so-far unrecognized quality control mechanism involving BAG3, HSPB8 and p62/SQSTM1 for accurate remodelling of actin-based mitotic structures that guide spindle orientation.

Indexed as

Actin CytoskeletonAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsAutophagyChromosome SegregationConcanavalin AHeat-Shock ProteinsHeat-Shock ResponseHeLa CellsHumansMCF-7 CellsMitosisMolecular ChaperonesProtein BindingProtein Serine-Threonine KinasesProteolysisAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsBAG3 protein, humanConcanavalin AHeat-Shock ProteinsHSPB8 protein, humanMolecular ChaperonesProtein Serine-Threonine KinasesRNA, Small InterferingSequestosome-1 ProteinSQSTM1 protein, human

Identifiers

PMID26496431
PMCPMC4619738
OpenAlexW1783583538

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.